Evidence map›Paper›PMID 16923829›Full record

ArticleThe Journal of cell biology2006

Sumoylation of the budding yeast kinetochore protein Ndc10 is required for Ndc10 spindle localization and regulation of anaphase spindle elongation.

Ben Montpetit, Tony R Hazbun, Stanley Fields, Philip Hieter

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.0field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

52 citing papers in PubMed, 84 citations in OpenAlex.

  1. Review
  2. Article
  3. Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024
    Review
  4. Article
  5. Article
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  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. The SUMO Pathway in Mitosis.Advances in experimental medicine and biology · 2017
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 4 institutions in 3 countries.

Ben MontpetitMichael Smith Laboratories, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada.
Tony R Hazbun
Stanley Fields
Philip Hieter
Howard Hughes Medical Institute · USPurdue University West Lafayette · USUniversity of British Columbia · CAUpsher-Smith Laboratories (United Kingdom) · GB

Funding

ZDS2P REGULATES SWE1P-DEPENDENT POLARIZED CELL GROWTH IN S CEREVISIAEP41RR011823 · NCRR · UNIVERSITY OF WASHINGTON · PI DAVIS, TRACY · 1996 to 2011
$24.7M
NCI NIH HHS P01-CA0161519NCRR NIH HHS P41 RR011823NCRR NIH HHS P41 RR11823
6 · The paper itself

Abstract

Posttranslational modification by the ubiquitin-like protein SUMO (small ubiquitin-like modifier) is emerging as an important regulator in many cellular processes, including genome integrity. In this study, we show that the kinetochore proteins Ndc10, Bir1, Ndc80, and Cep3, which mediate the attachment of chromosomes to spindle microtubules, are sumoylated substrates in budding yeast. Furthermore, we show that Ndc10, Bir1, and Cep3 but not Ndc80 are desumoylated upon exposure to nocodazole, highlighting the possibility of distinct roles for sumoylation in modulating kinetochore protein function and of a potential link between the sumoylation of kinetochore proteins and mitotic checkpoint function. We find that lysine to arginine mutations that eliminate the sumoylation of Ndc10 cause chromosome instability, mislocalization of Ndc10 from the mitotic spindle, abnormal anaphase spindles, and a loss of Bir1 sumoylation. These data suggest that sumoylation of Ndc10 and other kinetochore proteins play a critical role during the mitotic process.

Indexed as

AnaphaseProtein Processing, Post-TranslationalBenomylChromosomal InstabilityDNA-Binding ProteinsFungal ProteinsKinetochoresLysineMating FactorMutationNocodazoleNuclear ProteinsPeptidesProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsBenomylCBF2 protein, S cerevisiaeCEP3 protein, S cerevisiaeDNA-Binding ProteinsFungal ProteinsLysineMating FactorNDC80 protein, S cerevisiaeNocodazoleNuclear ProteinsPeptidesSaccharomyces cerevisiae ProteinsSmall Ubiquitin-Related Modifier Proteins

Identifiers

PMID16923829
PMCPMC2064309
OpenAlexW2138226364

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.